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- W2022166590 endingPage "1029" @default.
- W2022166590 startingPage "1021" @default.
- W2022166590 abstract "Na,K-ATPase, an alpha, beta heterodimer, is found in the plasma membrane of all animal cells. The alpha chain is believed to have 10 transmembrane regions and a large cytoplasmic domain between the 4th and 5th transmembrane regions (H4-H5). In our previous report, the large (3rd) cytoplasmic domains of the alpha1 and alpha2 isoform were found to interact with cofilin, an actin-modulating protein, by the yeast two-hybrid system. Here we show that cofilin interacts only with the 3rd cytoplasmic domain of the alpha2 subunit but not with the 2nd, 4th, and 5th cytoplasmic domains or the cytoplasmic region of the beta subunit of Na,K-ATPase. We also demonstrate that cofilin interacts with the large cytoplasmic domains of the alpha1, alpha2 and alpha3 isoforms of Na,K-ATPase, but not with those of glucose transporter 1, glucose transporter 4, cystic fibrosis transmembrane conductance regulator and plasma membrane Ca-ATPase. We introduced 10 mutations into the 3rd cytoplasmic domain of Na,K-ATPase to identify the binding sites with cofilin. Eight of these mutants were single amino acid substitutions (R417Q, K470Q, K654G, D672A, K691A, R700G, R700A and D710G) and two were double mutant (K654GR700G and K719AK720A). Analysis of the activity of the reporter gene of these mutants shows that residues D672 and R700 of the 3rd cytoplasmic domain of Na,K-ATPase are involved in the interaction with cofilin." @default.
- W2022166590 created "2016-06-24" @default.
- W2022166590 creator A5012978275 @default.
- W2022166590 creator A5031370310 @default.
- W2022166590 creator A5031635205 @default.
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- W2022166590 date "2002-10-01" @default.
- W2022166590 modified "2023-10-03" @default.
- W2022166590 title "Identification of the cofilin-binding sites in the large cytoplasmic domain of Na,K-ATPase" @default.
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- W2022166590 doi "https://doi.org/10.1016/s0300-9084(02)00004-4" @default.
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